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KCT2_PONAB
ID   KCT2_PONAB              Reviewed;         265 AA.
AC   Q5R5B8;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Keratinocyte-associated transmembrane protein 2;
DE   Flags: Precursor;
GN   Name=KCT2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
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DR   EMBL; CR860944; CAH93048.1; -; mRNA.
DR   RefSeq; NP_001126803.1; NM_001133331.1.
DR   AlphaFoldDB; Q5R5B8; -.
DR   STRING; 9601.ENSPPYP00000017646; -.
DR   GeneID; 100173807; -.
DR   KEGG; pon:100173807; -.
DR   CTD; 101940557; -.
DR   eggNOG; ENOG502S2NF; Eukaryota.
DR   InParanoid; Q5R5B8; -.
DR   OrthoDB; 1364680at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR037645; KCT2.
DR   PANTHER; PTHR16502; PTHR16502; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..49
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..265
FT                   /note="Keratinocyte-associated transmembrane protein 2"
FT                   /id="PRO_0000019581"
FT   TOPO_DOM        50..196
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          72..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC54"
FT   MOD_RES         256
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC54"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   265 AA;  29182 MW;  FA78502A836BF087 CRC64;
     MAAAALKRMR GPAQAKLLPG SAIQALVGLA RPLVLALLLV SAALSSVVSR TDSPSPTVLN
     SHISTPNVNA LTHENQTKPS ISQISTTLPP TMSTEKSGGA SVAPHPSPTP LSQEEADNNE
     DPSIEEEDLL MLNSSPSTAK DTLDNGDYGE PDYDWTTGPR DDDESDDTLE ENRGYVEIEQ
     SVKSFKMPSS NIEEEDSHFF FHLIIFAFCI AVVYITYHNK RKIFLLVQSR KWRDGLCSKT
     VEYHRLDQNV NEAMPSLKIT NDYTF
 
 
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